In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

WU Xu Li; WANG Wen Pu; XIA Li Xin; XU Hong; WU Hui; LIU Zhi Gang

doi:10.3967/0895-3988.2012.03.012

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Volume 25 Issue 3

Jun. 2012

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Article Navigation > Biomedical and Environmental Sciences > 2012 > 25(3): 334-339

WU Xu Li, WANG Wen Pu, XIA Li Xin, XU Hong, WU Hui, LIU Zhi Gang. In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method[J]. Biomedical and Environmental Sciences, 2012, 25(3): 334-339. doi: 10.3967/0895-3988.2012.03.012

Citation:

WU Xu Li, WANG Wen Pu, XIA Li Xin, XU Hong, WU Hui, LIU Zhi Gang. In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method[J]. Biomedical and Environmental Sciences, 2012, 25(3): 334-339. doi: 10.3967/0895-3988.2012.03.012

In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

doi: 10.3967/0895-3988.2012.03.012

College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China; School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China
School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China
College of Chemistry and Chemical Engineering, Shenzhen University, Shenzhen 518060, Guangdong, China
College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China

Funds: This research was supported by the Natural Science Foundation of China(30871752)%the High-tech Industrialization Funding of Guangdong Province(2009B011300010)

Abstract

Objective To characterize the relationship between the refolding process of recombinant bovine β-lactoglobulin and its immunoreactivity for clinical purposes.To establish a spectral method which examine the extent of recombinant allergen renaturation.Methods The refolding process of recombinant bovine β-lactoglobulin was investigated by using circular dichroism,fluorescence and synchronous fluorescence spectra.IgE-binding capacity of recombinant protein was analyzed by ELISA.In addition,bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro.Results Renaturation of recombinant bovine β-lactoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity.Conclusion The degree of protein renaturation correlated with the IgE-binding capacity of the protein.Results from this study may be of help for food allergy therapy and development of vaccination in the future.
- Food allergen,
- β-Lactoglobulin,
- Protein folding,
- Spectroscopy,
- Immunoreactivity
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通讯作者: 陈斌, bchen63@163.com

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沈阳化工大学材料科学与工程学院沈阳 110142

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In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

doi: 10.3967/0895-3988.2012.03.012

College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China; School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China

School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China

College of Chemistry and Chemical Engineering, Shenzhen University, Shenzhen 518060, Guangdong, China

College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China

Funds: This research was supported by the Natural Science Foundation of China(30871752)%the High-tech Industrialization Funding of Guangdong Province(2009B011300010)

Key words:

Abstract: Objective To characterize the relationship between the refolding process of recombinant bovine β-lactoglobulin and its immunoreactivity for clinical purposes.To establish a spectral method which examine the extent of recombinant allergen renaturation.Methods The refolding process of recombinant bovine β-lactoglobulin was investigated by using circular dichroism,fluorescence and synchronous fluorescence spectra.IgE-binding capacity of recombinant protein was analyzed by ELISA.In addition,bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro.Results Renaturation of recombinant bovine β-lactoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity.Conclusion The degree of protein renaturation correlated with the IgE-binding capacity of the protein.Results from this study may be of help for food allergy therapy and development of vaccination in the future.

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